ID PGES2_HUMAN Reviewed; 377 AA. AC Q9H7Z7; Q53EW9; Q5SYV6; Q96GI0; Q96GL2; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 24-JAN-2024, entry version 190. DE RecName: Full=Prostaglandin E synthase 2; DE EC=5.3.99.3 {ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783, ECO:0000269|PubMed:18198127}; DE AltName: Full=Membrane-associated prostaglandin E synthase-2 {ECO:0000303|PubMed:12804604}; DE Short=mPGE synthase-2 {ECO:0000303|PubMed:12804604}; DE AltName: Full=Microsomal prostaglandin E synthase 2; DE Short=mPGES-2; DE AltName: Full=Prostaglandin-H(2) E-isomerase; DE Contains: DE RecName: Full=Prostaglandin E synthase 2 truncated form; GN Name=PTGES2; Synonyms=C9orf15, PGES2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP TISSUE SPECIFICITY. RX PubMed=11866447; DOI=10.1006/bbrc.2002.6531; RA Tanikawa N., Ohmiya Y., Ohkubo H., Hashimoto K., Kangawa K., Kojima M., RA Ito S., Watanabe K.; RT "Identification and characterization of a novel type of membrane-associated RT prostaglandin E synthase."; RL Biochem. Biophys. Res. Commun. 291:884-889(2002). RN [6] RP CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-110 AND CYS-113, ACTIVITY RP REGULATION, AND FUNCTION. RX PubMed=12804604; DOI=10.1016/s0006-291x(03)01025-8; RA Watanabe K., Ohkubo H., Niwa H., Tanikawa N., Koda N., Ito S., Ohmiya Y.; RT "Essential 110Cys in active site of membrane-associated prostaglandin E RT synthase-2."; RL Biochem. Biophys. Res. Commun. 306:577-581(2003). RN [7] RP PROTEOLYTIC CLEAVAGE, AND SUBCELLULAR LOCATION. RX PubMed=12835322; DOI=10.1074/jbc.m305108200; RA Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T., RA Ohmiya Y., Watanabe K., Kudo I.; RT "Cellular prostaglandin E2 production by membrane-bound prostaglandin E RT synthase-2 via both cyclooxygenases-1 and -2."; RL J. Biol. Chem. 278:37937-37947(2003). RN [8] RP INTERACTION WITH EXOSC10. RX PubMed=15231747; DOI=10.1101/gr.2122004; RA Lehner B., Sanderson C.M.; RT "A protein interaction framework for human mRNA degradation."; RL Genome Res. 14:1315-1323(2004). RN [9] RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF CYS-110. RX PubMed=17585783; DOI=10.1021/bi700605m; RA Yamada T., Takusagawa F.; RT "PGH2 degradation pathway catalyzed by GSH-heme complex bound microsomal RT prostaglandin E2 synthase type 2: the first example of a dual-function RT enzyme."; RL Biochemistry 46:8414-8424(2007). RN [10] RP FUNCTION, CATALYTIC ACTIVITY, AND CAUTION. RX PubMed=18198127; DOI=10.1016/j.bbrc.2008.01.029; RA Watanabe K., Ito S., Yamamoto S.; RT "Studies on membrane-associated prostaglandin E synthase-2 with reference RT to production of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT)."; RL Biochem. Biophys. Res. Commun. 367:782-786(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Isomerase that catalyzes the conversion of PGH2 into the more CC stable prostaglandin E2 (PGE2) (in vitro) (PubMed:12804604, CC PubMed:18198127, PubMed:17585783). The biological function and the GSH- CC dependent property of PTGES2 is still under debate (PubMed:18198127, CC PubMed:17585783). In vivo, PTGES2 could form a complex with GSH and CC heme and would not participate in PGE2 synthesis but would catalyze the CC degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy- CC 5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) CC (PubMed:17585783) (By similarity). {ECO:0000250|UniProtKB:Q9N0A4, CC ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783, CC ECO:0000269|PubMed:18198127}. CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin H2 = prostaglandin E2; Xref=Rhea:RHEA:12893, CC ChEBI:CHEBI:57405, ChEBI:CHEBI:606564; EC=5.3.99.3; CC Evidence={ECO:0000269|PubMed:12804604, ECO:0000269|PubMed:17585783, CC ECO:0000269|PubMed:18198127}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12894; CC Evidence={ECO:0000305|PubMed:12804604}; CC -!- CATALYTIC ACTIVITY: CC Reaction=prostaglandin H2 = (12S)-hydroxy-(5Z,8E,10E)- CC heptadecatrienoate + malonaldehyde; Xref=Rhea:RHEA:48644, CC ChEBI:CHEBI:57405, ChEBI:CHEBI:90694, ChEBI:CHEBI:566274; CC Evidence={ECO:0000269|PubMed:17585783}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48645; CC Evidence={ECO:0000305|PubMed:17585783}; CC -!- ACTIVITY REGULATION: Isomerase activity is increased by sulfhydril CC compounds. Dithiothreitol (DTT) is most effective, followed by CC dihydrolipoic acid, glutathione (GSH) and 2-mercaptoethanol. CC {ECO:0000269|PubMed:12804604}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=56 uM for PGH2 (for the GSH-heme complex-bound enzyme) CC {ECO:0000269|PubMed:17585783}; CC -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis. CC -!- SUBUNIT: Homodimer. May interact with CEBPB (By similarity). Interacts CC with EXOSC10. {ECO:0000250|UniProtKB:Q66LN0, CC ECO:0000250|UniProtKB:Q8BWM0, ECO:0000269|PubMed:15231747}. CC -!- INTERACTION: CC Q9H7Z7; Q5VU69: CFAP141; NbExp=3; IntAct=EBI-681645, EBI-10247920; CC Q9H7Z7; PRO_0000449625 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-681645, EBI-25475871; CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:12835322}; Single-pass membrane protein CC {ECO:0000255}. CC -!- SUBCELLULAR LOCATION: [Prostaglandin E synthase 2 truncated form]: CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:12835322}. CC Note=Synthesized as a Golgi membrane-bound protein, which is further CC cleaved into the predominant soluble truncated form. The truncated form CC is cytoplasmic and is enriched in the perinuclear region. CC {ECO:0000269|PubMed:12835322}. CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the heart, including CC apex, inter-ventricular septum, both atria and ventricles, but not in CC the aorta. Also expressed in fetal heart. Detected in various regions CC of the brain: cerebellum; occipital, frontal and parietal lobes. Also CC expressed in the lymph nodes, skeletal muscle, kidney and trachea, but CC not in the thymus or lung. Overexpressed in colorectal cancer. CC {ECO:0000269|PubMed:11866447}. CC -!- PTM: Synthesized as a Golgi membrane-associated protein, and the CC proteolytic removal of the N-terminal hydrophobic domain leads to the CC formation of a mature cytosolic enzyme. {ECO:0000269|PubMed:12835322}. CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}. CC -!- CAUTION: It is not known if heme and GST are required for prostaglandin CC synthase activity. The protein copurifies with heme and GST when DTT is CC omitted during the purification procedure. The GSH-heme complex-bound CC enzyme has been proposed to act as a lyase and catalyze the degradation CC of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)- CC heptadecatrienoic acid (HHT) and malondialdehyde (MDA). According to CC PubMed:18198127, boiling the enzyme leads to loss of prostaglandin CC synthase activity, but does not eliminate the lyase activity. Besides, CC free heme can catalyze the formation of 12L-hydroxy-5,8,10- CC heptadecatrienoic acid (HHT) (PubMed:18198127). A more recent study CC demonstrates the GSH-dependent property of PTGES2, DTT dissociates the CC bound heme to produce active PGE2 synthase in vitro (By similarity). CC PTGES2 can only catalyzes PGE2 synthesis in the free state as an CC enzyme, while in vivo it forms a complex with heme and does not CC participate in PGE2 synthesis (By similarity). In agreement with this CC study, the in vivo evidence from PTGES2 deficient mice do not show that CC this protein is responsible for the PGE2 production under basal or CC pathophysiological conditions (By similarity). CC {ECO:0000250|UniProtKB:Q8BWM0, ECO:0000250|UniProtKB:Q9N0A4, CC ECO:0000269|PubMed:18198127, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK024100; BAB14826.1; -; mRNA. DR EMBL; AK223520; BAD97240.1; -; mRNA. DR EMBL; AL590708; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009397; AAH09397.2; -; mRNA. DR EMBL; BC009456; AAH09456.1; -; mRNA. DR EMBL; BC011613; AAH11613.1; -; mRNA. DR CCDS; CCDS6891.1; -. DR RefSeq; NP_001243264.1; NM_001256335.1. DR RefSeq; NP_079348.1; NM_025072.6. DR RefSeq; NP_945176.1; NM_198938.2. DR AlphaFoldDB; Q9H7Z7; -. DR SMR; Q9H7Z7; -. DR BioGRID; 123135; 96. DR IntAct; Q9H7Z7; 29. DR MINT; Q9H7Z7; -. DR STRING; 9606.ENSP00000345341; -. DR BindingDB; Q9H7Z7; -. DR ChEMBL; CHEMBL4411; -. DR GuidetoPHARMACOLOGY; 1378; -. DR SwissLipids; SLP:000001095; -. DR GlyGen; Q9H7Z7; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H7Z7; -. DR MetOSite; Q9H7Z7; -. DR PhosphoSitePlus; Q9H7Z7; -. DR SwissPalm; Q9H7Z7; -. DR BioMuta; PTGES2; -. DR DMDM; 73921741; -. DR EPD; Q9H7Z7; -. DR jPOST; Q9H7Z7; -. DR MassIVE; Q9H7Z7; -. DR MaxQB; Q9H7Z7; -. DR PaxDb; 9606-ENSP00000345341; -. DR PeptideAtlas; Q9H7Z7; -. DR ProteomicsDB; 81164; -. DR Pumba; Q9H7Z7; -. DR TopDownProteomics; Q9H7Z7; -. DR Antibodypedia; 17330; 376 antibodies from 34 providers. DR DNASU; 80142; -. DR Ensembl; ENST00000338961.11; ENSP00000345341.6; ENSG00000148334.16. DR GeneID; 80142; -. DR KEGG; hsa:80142; -. DR MANE-Select; ENST00000338961.11; ENSP00000345341.6; NM_025072.7; NP_079348.1. DR UCSC; uc004bti.4; human. DR AGR; HGNC:17822; -. DR CTD; 80142; -. DR DisGeNET; 80142; -. DR GeneCards; PTGES2; -. DR HGNC; HGNC:17822; PTGES2. DR HPA; ENSG00000148334; Low tissue specificity. DR MIM; 608152; gene. DR neXtProt; NX_Q9H7Z7; -. DR OpenTargets; ENSG00000148334; -. DR PharmGKB; PA33949; -. DR VEuPathDB; HostDB:ENSG00000148334; -. DR eggNOG; KOG3029; Eukaryota. DR GeneTree; ENSGT00390000000224; -. DR HOGENOM; CLU_011226_0_0_1; -. DR InParanoid; Q9H7Z7; -. DR OMA; DYCLTEG; -. DR OrthoDB; 1226at2759; -. DR PhylomeDB; Q9H7Z7; -. DR TreeFam; TF314304; -. DR BioCyc; MetaCyc:HS07514-MONOMER; -. DR BRENDA; 5.3.99.3; 2681. DR PathwayCommons; Q9H7Z7; -. DR Reactome; R-HSA-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX). DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; Q9H7Z7; -. DR SIGNOR; Q9H7Z7; -. DR UniPathway; UPA00662; -. DR BioGRID-ORCS; 80142; 20 hits in 1171 CRISPR screens. DR ChiTaRS; PTGES2; human. DR GeneWiki; PTGES2; -. DR GenomeRNAi; 80142; -. DR Pharos; Q9H7Z7; Tchem. DR PRO; PR:Q9H7Z7; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9H7Z7; Protein. DR Bgee; ENSG00000148334; Expressed in apex of heart and 188 other cell types or tissues. DR ExpressionAtlas; Q9H7Z7; baseline and differential. DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0036134; F:12-hydroxyheptadecatrienoic acid synthase activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:Ensembl. DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB. DR GO; GO:0020037; F:heme binding; ISS:UniProtKB. DR GO; GO:0016829; F:lyase activity; IDA:UniProtKB. DR GO; GO:0050220; F:prostaglandin-E synthase activity; IDA:FlyBase. DR GO; GO:0019371; P:cyclooxygenase pathway; TAS:Reactome. DR GO; GO:0006629; P:lipid metabolic process; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl. DR GO; GO:0046903; P:secretion; IEA:Ensembl. DR CDD; cd03197; GST_C_mPGES2; 1. DR CDD; cd03040; GST_N_mPGES2; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 6.20.200.30; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR034334; PGES2. DR InterPro; IPR034335; PGES2_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR12782; MICROSOMAL PROSTAGLANDIN E SYNTHASE-2; 1. DR PANTHER; PTHR12782:SF5; PROSTAGLANDIN E SYNTHASE 2; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF13417; GST_N_3; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01203; Prostaglandin_E_synthase_like1; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS00195; GLUTAREDOXIN_1; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. DR PROSITE; PS50405; GST_CTER; 1. DR Genevisible; Q9H7Z7; HS. PE 1: Evidence at protein level; KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism; Golgi apparatus; KW Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Phosphoprotein; KW Prostaglandin biosynthesis; Prostaglandin metabolism; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..377 FT /note="Prostaglandin E synthase 2" FT /id="PRO_0000013127" FT CHAIN 88..377 FT /note="Prostaglandin E synthase 2 truncated form" FT /evidence="ECO:0000250|UniProtKB:Q66LN0" FT /id="PRO_0000013128" FT TOPO_DOM 1..57 FT /note="Lumenal" FT /evidence="ECO:0000255" FT TRANSMEM 58..74 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 75..377 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 90..193 FT /note="Glutaredoxin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686" FT DOMAIN 263..377 FT /note="GST C-terminal" FT BINDING 148 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:Q9N0A4" FT BINDING 164..165 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000250|UniProtKB:Q9N0A4" FT SITE 87..88 FT /note="Cleavage" FT /evidence="ECO:0000250|UniProtKB:Q66LN0" FT MOD_RES 95 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VARIANT 298 FT /note="R -> H (in dbSNP:rs13283456)" FT /id="VAR_049494" FT MUTAGEN 110 FT /note="C->S: Loss of prostaglandin-E synthase activity. Can FT bind glutathione-heme and exhibits PGH2 degradation FT activity." FT /evidence="ECO:0000269|PubMed:12804604, FT ECO:0000269|PubMed:17585783" FT MUTAGEN 113 FT /note="C->S: Slightly decreased prostaglandin-E synthase FT activity." FT /evidence="ECO:0000269|PubMed:12804604" FT CONFLICT 319 FT /note="G -> S (in Ref. 2; BAD97240)" FT /evidence="ECO:0000305" SQ SEQUENCE 377 AA; 41943 MW; 82F2DF867BB8337C CRC64; MDPAARVVRA LWPGGCALAW RLGGRPQPLL PTQSRAGFAG AAGGPSPVAA ARKGSPRLLG AAALALGGAL GLYHTARWHL RAQDLHAERS AAQLSLSSRL QLTLYQYKTC PFCSKVRAFL DFHALPYQVV EVNPVRRAEI KFSSYRKVPI LVAQEGESSQ QLNDSSVIIS ALKTYLVSGQ PLEEIITYYP AMKAVNEQGK EVTEFGNKYW LMLNEKEAQQ VYGGKEARTE EMKWRQWADD WLVHLISPNV YRTPTEALAS FDYIVREGKF GAVEGAVAKY MGAAAMYLIS KRLKSRHRLQ DNVREDLYEA ADKWVAAVGK DRPFMGGQKP NLADLAVYGV LRVMEGLDAF DDLMQHTHIQ PWYLRVERAI TEASPAH //